Multi-spanning membrane proteins: how accurate are the models?
about
Statistical distribution of hydrophobic residues along the length of protein chains. Implications for protein folding and evolution.Molecular cloning and chromosomal localization of one of the human glutamate receptor genesInteraction of a permeant maleimide derivative of cysteine with the erythrocyte glucose carrier. Differential labelling of an exofacial carrier thiol group and its role in the transport mechanismComplementation of a glucose transporter mutant of Schizosaccharomyces pombe by a novel Trypanosoma brucei gene.Isolation and characterization of the LGT1 gene encoding a low-affinity glucose transporter from Torulaspora delbrueckii.A single nonpolar residue in the deep pore of related K+ channels acts as a K+:Rb+ conductance switchStructure and function of the glycine receptor and related nicotinicoid receptors.Nobel lecture. A structural basis of light energy and electron transfer in biologySequence and structure of the yeast galactose transporterStructural and functional dissection of Sec62p, a membrane-bound component of the yeast endoplasmic reticulum protein import machinery.Anion-exchange mechanisms in bacteria.Membrane topology analysis of Escherichia coli mannitol permease by using a nested-deletion method to create mtlA-phoA fusionsEffects of deletions in the carboxy-terminal hydrophobic region of herpes simplex virus glycoprotein gB on intracellular transport and membrane anchoring.Yeast sugar transporters.High resolution 1H NMR study of the solution structure of the S4 segment of the sodium channel protein.Transmembrane segments of the P-type cation-transporting ATPases. A comparative study.
P2860
Q24537384-7A22ED33-C907-4FC9-80BE-5804A913DC80Q24563078-8FBB25B3-32AE-4AA8-B236-3DBFAE947D29Q28340568-ABB81CCA-6C0E-40FB-90C5-6D3B96D06D6BQ30649968-A31CB2D9-642A-4FF6-9E85-BA5CD18FCE0CQ33211731-2C8BA5FF-4D6E-4B7D-A927-BE5B75A9D9B7Q34089105-F158CB52-7488-4B22-A70F-B9A203EE6AA2Q34306215-FB2DEE62-44A2-416E-993C-48E476A322F2Q34675237-B1621294-DE0B-4C20-9970-B326A2E41000Q36180947-B8652F94-B935-41A2-B3A2-7F281CAEA9B6Q36733719-62C47C4D-31E6-42CB-ABF7-10A87276C49CQ37056022-435BC174-4B17-4894-A4A2-62C6D446B6D9Q37611477-7784A89D-C5F4-4B5B-A16C-343B70041131Q40046543-D60677DC-55AF-45B5-A564-FEC2A94DD9EFQ40861734-B3726E83-C7DB-4D6A-8F08-C4F53150620AQ41812721-37E045D0-CF93-425D-9CEC-19BB23D337DAQ54736610-0D878543-6280-40EA-9CF5-15C51DC403B0
P2860
Multi-spanning membrane proteins: how accurate are the models?
description
article científic
@ca
article scientifique
@fr
articol științific
@ro
articolo scientifico
@it
artigo científico
@gl
artigo científico
@pt
artigo científico
@pt-br
artikel ilmiah
@id
artikull shkencor
@sq
artículo científico
@es
name
Multi-spanning membrane proteins: how accurate are the models?
@en
type
label
Multi-spanning membrane proteins: how accurate are the models?
@en
prefLabel
Multi-spanning membrane proteins: how accurate are the models?
@en
P1476
Multi-spanning membrane proteins: how accurate are the models?
@en
P304
P356
10.1016/0968-0004(88)90101-6
P577
1988-09-01T00:00:00Z